Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints

J Biomol NMR. 2014 Sep;60(1):67-71. doi: 10.1007/s10858-014-9852-0. Epub 2014 Aug 8.

Abstract

MerF is a mercury transport membrane protein from the bacterial mercury detoxification system. By performing a solid-state INEPT experiment and measuring chemical shift anisotropy frequencies in aligned samples, we are able to improve on the accuracy and precision of the initial structure that we presented. MerF has four N-terminal and eleven C-terminal residues that are mobile and unstructured in phospholipid bilayers. The structure presented here has average pairwise RMSDs of 1.78 Å for heavy atoms and 0.92 Å for backbone atoms.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Anisotropy
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Cation Transport Proteins / chemistry*
  • Cation Transport Proteins / metabolism
  • Escherichia coli / metabolism
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Cation Transport Proteins
  • MerF mercury transport protein, Pseudomonas fluorescens
  • Recombinant Proteins